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From Wikipedia, the free encyclopedia
The enzyme polynucleotide 5′-phosphatase (RNA 5′-triphosphatase, RTPase, EC 3.1.3.33) is an enzyme that catalyzes the reaction
polynucleotide 5′-phosphatase | |||||||||
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Identifiers | |||||||||
EC no. | 3.1.3.33 | ||||||||
CAS no. | 37288-17-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is polynucleotide 5′-phosphohydrolase. This enzyme is also called 5′-polynucleotidase.
The only specific molecular function known is the catalysis of the reaction:
RTPases cleave the 5′-terminal γ-β phosphoanhydride bond of nascent messenger RNA molecules, enabling the addition of a five-prime cap as part of post-transcriptional modifications. RTPases generate 5′-diphosphate-ended mRNA and a phosphate ion from 5′-triphosphate-ended precursor mRNA. mRNA guanylyltransferase then adds a backwards guanosine monophosphate (GMP) group from GTP, generating pyrophosphate, and mRNA (guanine-N7-)-methyltransferase methylates the guanine to form the final 5′-cap structure.[1][2][3][4][5]
There are two families of RTPases known so far:
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1D8H, 1D8I, 1I9S, 1I9T, and 1YN9.
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